Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Brian M. Beyer"'
Autor:
Brian M. Beyer, Vincent Madison, Eric M. Parker, Mckittrick Brian A, Daniel F. Wyss, William J. Greenlee, Corey Strickland, T. Nechuta, Johannes H. Voigt, John C. Hunter, Mary M. Senior, Andrew Stamford, Matthew E. Kennedy, Michael Czarniecki, Yu-Sen Wang, Elizabeth M. Smith
Publikováno v:
Journal of Medicinal Chemistry. 53:942-950
Fragment-based NMR screening, X-ray crystallography, structure-based design, and focused chemical library design were used to identify novel inhibitors for BACE-1. A rapid optimization of an initial NMR hit was achieved by a combination of NMR and a
Autor:
Paul Reichert, Peter Orth, Lata Ramanathan, Hung V. Le, Brian M. Beyer, Vincent Madison, Richard N. Ingram
Publikováno v:
Journal of Molecular Biology. 382:942-955
Interleukin (IL)-23 is a pro-inflammatory cytokine playing a key role in the pathogenesis of several autoimmune and inflammatory diseases. We have determined the crystal structures of the heterodimeric p19-p40 IL-23 and its complex with the Fab (anti
Autor:
Liu Yi-Tsung, Frank Bennett, Viyyoor M. Girijavallabhan, F. George Njoroge, Lata Ramanathan, John Pichardo, Kevin X. Chen, S. Shane Taremi, Andrew Prongay, Brian M. Beyer, Corey Strickland, Rumin Zhang, Vincent Madison, Edwin Jao, Zhuyan Guo, Zhi Hong, Patricia C. Weber, Anil K. Saksena, Stephane L. Bogen, Srikanth Venkatraman, Rong-Sheng Yang, Nanhua Yao, Joseph E. Myers, Bruce A. Malcolm, Taisa Yarosh-Tomaine, Raymond G. Lovey, Richard N. Ingram, Ashok Arasappan, Thierry O. Fischmann, Mary M. Senior, Winifred W. Prosise
Publikováno v:
Journal of Synchrotron Radiation
Crystal structures of protease/inhibitor complexes guided optimization of the buried nonpolar surface area thereby maximizing hydrophobic binding. The resulting potent tripeptide inhibitor is in clinical trials.
The structures of both native and
The structures of both native and
Autor:
Mckittrick Brian A, Richard N. Ingram, Daniel Lundell, Peter Orth, Robert Mazzola, Zhuyan Guo, Xiaoda Niu, Jing Sun, Brian M. Beyer, Vincent Madison, Zhaoning Zhu, Lisa Sinning
Publikováno v:
Journal of Medicinal Chemistry. 51:725-736
Through a de novo design approach, hydroxamates derived from trans-cyclopropyl dicarboxylate were examined as potential TNF-alpha converting enzyme (TACE) inhibitors. Two distinctive series of inhibitors (A and B) were identified and shown to have di
Autor:
Nanhua Yao, Lata Ramanathan, Kevin X. Chen, Thierry O. Fischmann, Andrew Prongay, Corey Strickland, Mary M. Senior, Raymond G. Lovey, Richard N. Ingram, Bruce A. Malcolm, Viyyoor M. Girijavallabhan, Frank Bennett, Patricia C. Weber, Taisa Yarosh-Tomaine, John Pichardo, Anil K. Saksena, F. George Njoroge, Rong-Sheng Yang, Zhuyan Guo, Zhi Hong, Stephane L. Bogen, Srikanth Venkatraman, Ashok Arasappan, S. Shane Taremi, Brian M. Beyer, Rumin Zhang, Vincent Madison, Edwin Jao, Winifred W. Prosise, Yi-Tsung Liu, Joseph E. Myers
Publikováno v:
Journal of Medicinal Chemistry. 50:2310-2318
The structures of both the native holo-HCV NS3/4A protease domain and the protease domain with a serine 139 to alanine (S139A) mutation were solved to high resolution. Subsequently, structures were...
Publikováno v:
Biochemistry. 44:16594-16601
Accumulation of the cytotoxic 40- to 42-residue beta-amyloid peptide represents the primary pathological process in Alzheimer's disease (AD). BACE1 (beta-site APP cleaving enzyme 1) is responsible for the initial required step in the neuronal amyloid
Autor:
Brian M. Beyer, Wenyan Wang, Julie Lee, Lili Zhang, S. Shane Taremi, Hung V. Le, Paul Reichert, Corey Strickland, JianJun Liu, Yan-Hui Liu
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1698:255-259
Human beta-amyloid precursor protein cleaving enzyme (beta-secretase, or BACE) belongs to the aspartyl protease family, and is responsible for generating the N-terminus of beta-amyloid peptide (Abeta). BACE is a type I transmembrane glycoprotein with
Autor:
Daniel F. Wyss, F. George Njoroge, Brian M. Beyer, Mark A. McCoy, Yu-Sen Wang, Mary M. Senior, Ashok Arasappan
Publikováno v:
Journal of Medicinal Chemistry. 47:2486-2498
NMR-based screening of a customized fragment library identified 16 small-molecule hits that bind weakly (K(D) approximately 100 microM to 10 mM) to substrate binding sites of the NS4A-bound NS3 protease of the hepatitis C virus (HCV). Analogues for f
Publikováno v:
Proteins: Structure, Function, and Genetics. 43:82-88
A comparison of the DNA sequences from all available genotypes of HCV indicate that the active site residues of the NS3 protease are strictly conserved with the exception of positions 123 and 168, which border the S4 subsite. In genotype 3, the canon
Autor:
Ben M. Dunn, Brian M. Beyer
Publikováno v:
Protein Science. 7:88-95
In order to contribute to our understanding of cathepsin D (CatD) active site specificity, two series of chromogenic octapeptides with systematic substitutions in positions P2' and P3' were synthesized. This panel was characterized with native human